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TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)

 TGFR1_PIG               Reviewed;         503 AA.
Q5CD18; Q5CD19;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 1.
16-OCT-2019, entry version 108.
RecName: Full=TGF-beta receptor type-1;
Short=TGFR-1;
EC=2.7.11.30;
AltName: Full=TGF-beta type I receptor;
AltName: Full=Transforming growth factor-beta receptor type I;
Short=TGF-beta receptor type I;
Short=TbetaR-I;
Flags: Precursor;
Name=TGFBR1;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS SER-8 AND
VAL-417.
TISSUE=Testis;
PubMed=16341765; DOI=10.1007/s10528-005-8165-0;
Shimanuki S., Mikawa A., Miyake Y., Hamasima N., Mikawa S., Awata T.;
"Structure and polymorphism analysis of transforming growth factor
beta receptor 1 (TGFBR1) in pigs.";
Biochem. Genet. 43:491-500(2005).
-!- FUNCTION: Transmembrane serine/threonine kinase forming with the
TGF-beta type II serine/threonine kinase receptor, TGFBR2, the
non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2
and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the
cell surface to the cytoplasm and is thus regulating a plethora of
physiological and pathological processes including cell cycle
arrest in epithelial and hematopoietic cells, control of
mesenchymal cell proliferation and differentiation, wound healing,
extracellular matrix production, immunosuppression and
carcinogenesis. The formation of the receptor complex composed of
2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the
cytokine dimer results in the phosphorylation and the activation
of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1
phosphorylates SMAD2 which dissociates from the receptor and
interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently
translocated to the nucleus where it modulates the transcription
of the TGF-beta-regulated genes. This constitutes the canonical
SMAD-dependent TGF-beta signaling cascade. Also involved in non-
canonical, SMAD-independent TGF-beta signaling pathways. For
instance, TGFBR1 induces TRAF6 autoubiquitination which in turn
results in MAP3K7 ubiquitination and activation to trigger
apoptosis. Also regulates epithelial to mesenchymal transition
through a SMAD-independent signaling pathway through PARD6A
phosphorylation and activation (By similarity).
{ECO:0000250|UniProtKB:P36897}.
-!- CATALYTIC ACTIVITY:
Reaction=[receptor-protein]-L-threonine + ATP = [receptor-
protein]-O-phospho-L-threonine + ADP + H(+);
Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-
COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.30;
-!- CATALYTIC ACTIVITY:
Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O-
phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA-
COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
ChEBI:CHEBI:456216; EC=2.7.11.30;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- ACTIVITY REGULATION: Kept in an inactive conformation by FKBP1A
preventing receptor activation in absence of ligand. CD109 is
another inhibitor of the receptor (By similarity).
{ECO:0000250|UniProtKB:P36897}.
-!- SUBUNIT: Homodimer; in the endoplasmic reticulum but also at the
cell membrane. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric
ligands assemble a functional receptor composed of two TGFBR1 and
TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The
respective affinity of TGBRB1 and TGFBR2 for the ligands may
modulate the kinetics of assembly of the receptor and may explain
the different biological activities of TGFB1, TGFB2 and TGFB3.
Interacts with CD109; inhibits TGF-beta receptor activation in
keratinocytes. Interacts with RBPMS. Interacts (unphosphorylated)
with FKBP1A; prevents TGFBR1 phosphorylation by TGFBR2 and
stabilizes it in the inactive conformation. Interacts with SMAD2,
SMAD3 and ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-beta
receptor. Interacts with TRAF6 and MAP3K7; induces MAP3K7
activation by TRAF6. Interacts with PARD6A; involved in TGF-beta
induced epithelial to mesenchymal transition. Interacts with
SMAD7, NEDD4L, SMURF1 and SMURF2; SMAD7 recruits NEDD4L, SMURF1
and SMURF2 to the TGF-beta receptor (By similarity). Interacts
with USP15 and VPS39. Interacts with SDCBP (via C-terminus).
Interacts with CAV1 and this interaction is impaired in the
presence of SDCBP (By similarity). Interacts with APPL1;
interaction is TGF beta dependent; mediates trafficking of the
TGFBR1 from the endosomes to the nucleus via microtubules in a
TRAF6-dependent manner (By similarity).
{ECO:0000250|UniProtKB:P36897}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P36897}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P36897}. Cell junction, tight
junction {ECO:0000250|UniProtKB:P36897}. Membrane raft
{ECO:0000250|UniProtKB:P36897}. Cell surface
{ECO:0000250|UniProtKB:P36897}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q5CD18-1; Sequence=Displayed;
Name=2;
IsoId=Q5CD18-2; Sequence=VSP_021594;
Note=May be due to a competing donor splice site.;
-!- PTM: Phosphorylated at basal levels in the absence of ligand.
Activated upon phosphorylation by TGFBR2, mainly in the GS domain.
Phosphorylation in the GS domain abrogates FKBP1A-binding (By
similarity). {ECO:0000250|UniProtKB:P36897}.
-!- PTM: N-Glycosylated. {ECO:0000250|UniProtKB:P36897}.
-!- PTM: Ubiquitinated; undergoes ubiquitination catalyzed by several
E3 ubiquitin ligases including SMURF1, SMURF2 and NEDD4L2. Results
in the proteasomal and/or lysosomal degradation of the receptor
thereby negatively regulating its activity. Deubiquitinated by
USP15, leading to stabilization of the protein and enhanced TGF-
beta signal. Its ubiquitination and proteasome-mediated
degradation is negatively regulated by SDCBP (By similarity).
{ECO:0000250|UniProtKB:P36897}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB182259; BAD91022.1; -; mRNA.
EMBL; AB182260; BAD91023.1; -; mRNA.
RefSeq; NP_001033728.1; NM_001038639.1. [Q5CD18-1]
STRING; 9823.ENSSSCP00000029422; -.
PaxDb; Q5CD18; -.
GeneID; 396665; -.
KEGG; ssc:396665; -.
CTD; 7046; -.
eggNOG; KOG2052; Eukaryota.
eggNOG; ENOG410XQT0; LUCA.
HOGENOM; HOG000230587; -.
InParanoid; Q5CD18; -.
KO; K04674; -.
OrthoDB; 776697at2759; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
GO; GO:0005623; C:cell; ISS:AgBase.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0016020; C:membrane; ISS:AgBase.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0048185; F:activin binding; IBA:GO_Central.
GO; GO:0016361; F:activin receptor activity, type I; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0046332; F:SMAD binding; IBA:GO_Central.
GO; GO:0050431; F:transforming growth factor beta binding; ISS:AgBase.
GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; ISS:AgBase.
GO; GO:0032924; P:activin receptor signaling pathway; ISS:AgBase.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
GO; GO:0042118; P:endothelial cell activation; ISS:AgBase.
GO; GO:0007507; P:heart development; ISS:AgBase.
GO; GO:0035556; P:intracellular signal transduction; ISS:AgBase.
GO; GO:0048762; P:mesenchymal cell differentiation; ISS:AgBase.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:AgBase.
GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:AgBase.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0010468; P:regulation of gene expression; ISS:AgBase.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:AgBase.
InterPro; IPR000472; Activin_recp.
InterPro; IPR003605; GS_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF01064; Activin_recp; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF08515; TGF_beta_GS; 1.
SMART; SM00467; GS; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51256; GS; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
Alternative splicing; Apoptosis; ATP-binding; Cell junction;
Cell membrane; Complete proteome; Differentiation; Disulfide bond;
Glycoprotein; Growth regulation; Isopeptide bond; Kinase; Magnesium;
Manganese; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Serine/threonine-protein kinase; Signal; Tight junction; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 29 {ECO:0000250}.
CHAIN 30 503 TGF-beta receptor type-1.
/FTId=PRO_0000260305.
TOPO_DOM 30 126 Extracellular. {ECO:0000255}.
TRANSMEM 127 147 Helical. {ECO:0000255}.
TOPO_DOM 148 503 Cytoplasmic. {ECO:0000255}.
DOMAIN 175 204 GS. {ECO:0000255|PROSITE-
ProRule:PRU00585}.
DOMAIN 205 495 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 211 219 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 193 194 FKBP1A-binding.
ACT_SITE 333 333 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 232 232 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000250|UniProtKB:P36897}.
MOD_RES 185 185 Phosphothreonine; by TGFBR2.
{ECO:0000250|UniProtKB:P36897}.
MOD_RES 186 186 Phosphothreonine; by TGFBR2.
{ECO:0000250|UniProtKB:P36897}.
MOD_RES 187 187 Phosphoserine; by TGFBR2.
{ECO:0000250|UniProtKB:P36897}.
MOD_RES 189 189 Phosphoserine; by TGFBR2.
{ECO:0000250|UniProtKB:P36897}.
MOD_RES 191 191 Phosphoserine; by TGFBR2.
{ECO:0000250|UniProtKB:P36897}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 32 50 {ECO:0000250|UniProtKB:P36897}.
DISULFID 34 37 {ECO:0000250|UniProtKB:P36897}.
DISULFID 44 67 {ECO:0000250|UniProtKB:P36897}.
DISULFID 82 96 {ECO:0000250|UniProtKB:P36897}.
DISULFID 97 102 {ECO:0000250|UniProtKB:P36897}.
CROSSLNK 391 391 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 111 114 Missing (in isoform 2).
{ECO:0000303|PubMed:16341765}.
/FTId=VSP_021594.
VARIANT 8 8 P -> S. {ECO:0000269|PubMed:16341765}.
VARIANT 417 417 I -> V. {ECO:0000269|PubMed:16341765}.
SEQUENCE 503 AA; 56174 MW; CFA1EEC793401A4A CRC64;
MEVAAGAPRS RLLLFVLAAT ATLAPEATAF QCFCHLCTKD NFTCVTDGLC FVSVTETTDK
VIHNSMCIAE IDLIPRDRPF VCAPSSKTGS VTTTYCCNQD HCNKIELPTV GPFPGKPPSG
LGPVELAAVI AGPVCFVCIS LMLMVYICHN RTVIHHRVPN EEDPSLDRPF ISEGTTLKDL
IYDMTTSGSG SGLPLLVQRT IARTIVLQES IGKGRFGEVW RGKWRGEEVA VKIFSSREER
SWFREAEIYQ TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD YLNRYTVTVE
GMIKLALSTA SGLAHLHMEI VGTQGKPAIA HRDLKSKNIL VKKNGTCCIA DLGLAVRHDS
ATDTIDIAPN HRVGTKRYMA PEVLDDSINM KHFESFKRAD IYAMGLVFWE IARRCSIGGI
HEDYQLPYYD LVPSDPSVEE MRKVVCEQKL RPNIPNRWQS CEALRVMAKI MRECWYANGA
ARLTALRIKK TLSQLSQQEG IKM


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[TGFB1 TGFB] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[MAP3K7 TAK1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[Map3k7 Tak1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB2] Transforming growth factor beta-2 proprotein (Cetermin) (Glioblastoma-derived T-cell suppressor factor) (G-TSF) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[TGFB3] Transforming growth factor beta-3 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-3 (TGF-beta-3)]
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Lefty1 Ebaf Lefty Stra3 Tgfb4] Left-right determination factor 1 (Protein lefty-1) (Lefty protein) (Stimulated by retinoic acid gene 3 protein) (Transforming growth factor beta-4) (TGF-beta-4)
[EIF3I EIF3S2 TRIP1] Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 subunit 2) (TGF-beta receptor-interacting protein 1) (TRIP-1) (eIF-3-beta) (eIF3 p36)
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Tgfbrap1] Transforming growth factor-beta receptor-associated protein 1 (TGF-beta receptor-associated protein 1) (TRAP-1) (TRAP1)
[TGFB2] Transforming growth factor beta-2 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)

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